Erratum to “Thermodynamic and Kinetic Characterization of Ligand Binding to the Purine Riboswitch Aptamer Domain” [J. Mol. Biol. 359 (2006) 754–768]

2006 ◽  
Vol 363 (2) ◽  
pp. 624 ◽  
Author(s):  
Sunny D. Gilbert ◽  
Colby D. Stoddard ◽  
Sarah J. Wise ◽  
Robert T. Batey
Keyword(s):  
Ligand Binding ◽  
Kinetic Characterization ◽  
Purine Riboswitch ◽  
Aptamer Domain

Thermodynamic and Kinetic Characterization of Ligand Binding to the Purine Riboswitch Aptamer Domain

2006 ◽  
Vol 359 (3) ◽  
pp. 754-768 ◽  
Author(s):  
Sunny D. Gilbert ◽  
Colby D Stoddard ◽  
Sarah J. Wise ◽  
Robert T. Batey
Keyword(s):  
Ligand Binding ◽  
Kinetic Characterization ◽  
Purine Riboswitch ◽  
Aptamer Domain

scholarly journals Structural basis for 2′-deoxyguanosine recognition by the 2′-dG-II class of riboswitches

2019 ◽  
Vol 47 (20) ◽  
pp. 10931-10941 ◽  
Author(s):  
Michal M Matyjasik ◽  
Robert T Batey
Keyword(s):  
Ligand Binding ◽  
Consensus Sequence ◽  
Bioinformatic Analysis ◽  
Binding Pocket ◽  
Structural Basis ◽  
Binding Core ◽  
Nucleotide Insertion ◽  
Parental Class ◽  
Purine Riboswitch ◽  
Aptamer Domain

Abstract A recent bioinformatic analysis of well-characterized classes of riboswitches uncovered subgroups unable to bind to the regulatory molecule of the parental class. Within the guanine/adenine class, seven groups of RNAs were identified that deviate from the consensus sequence at one or more of three positions directly involved purine nucleobase recognition, one of which was validated as a second class of 2′-deoxyguanosine riboswitch (called 2′-dG-II). To understand how 2′-dG-II riboswitches recognize their cognate ligand and how they differ from a previously identified class of 2′-deoxyguanosine binding riboswitches, we have solved the crystal structure of a 2′-dG-II aptamer domain bound to 2′-deoxyguanosine. This structure reveals a global architecture similar to other members of the purine riboswitch family, but contains key differences within the ligand binding core. Defining the 2′-dG-II riboswitches is a two-nucleotide insertion in the three-way junction that promotes novel base-base interactions. Unlike 2′-dG-I riboswitches, the 2′-dG-II class only requires local changes to the ligand binding pocket of the guanine/adenine class to achieve a change in ligand preference. Notably, members of the 2′-dG-II family have variable ability to discriminate between 2′-deoxyguanosine and riboguanosine, suggesting that a subset of 2′-dG-II riboswitches may bind either molecule to regulate gene expression.

Kinetic Characterization of Anticarsia gemmatalis Digestive Serine- Proteases and the Inhibitory Effect of Synthetic Peptides

2018 ◽  
Vol 24 (11) ◽  
Author(s):  
Adriana M. Patarroyo-Vargas ◽  
Yaremis B. Merino-Cabrera ◽  
Jose C. Zanuncio ◽  
Francelina Rocha ◽  
Wellington G. Campos ◽  
...  
Keyword(s):  
Synthetic Peptides ◽  
Serine Proteases ◽  
Inhibitory Effect ◽  
Anticarsia Gemmatalis ◽  
Kinetic Characterization

scholarly journals Kinetic characterization of yeast alcohol dehydrogenases. Amino acid residue 294 and substrate specificity.

1987 ◽  
Vol 262 (8) ◽  
pp. 3754-3761
Author(s):  
A.J. Ganzhorn ◽  
D.W. Green ◽  
A.D. Hershey ◽  
R.M. Gould ◽  
B.V. Plapp
Keyword(s):  
Amino Acid ◽  
Substrate Specificity ◽  
Amino Acid Residue ◽  
Kinetic Characterization ◽  
Alcohol Dehydrogenases
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